Evidence map›Paper›PMID 34163823›Full record

ArticleChemical science2021

Phase separation of p53 precedes aggregation and is affected by oncogenic mutations and ligands.

Elaine C Petronilho, Murilo M Pedrote, Mayra A Marques, Yulli M Passos, Michelle F Mota, Benjamin Jakobus, Gileno Dos Santos de Sousa, Filipe Pereira da Costa, Adriani L Felix, Giulia D S Ferretti and 5 more

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 citations in OpenAlex.

  1. Frontiers in neurology · 2024
    Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Transcription regulation by biomolecular condensates.Nature reviews. Molecular cell biology · 2025
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 2 institutions in 2 countries.

Elaine C PetronilhoInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Murilo M PedroteInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Mayra A MarquesInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.ORCID https://orcid.org/0000-0002-4131-4634
Yulli M PassosFaculty of Pharmacy, Federal University of Rio de Janeiro Rio de Janeiro Brazil.
Michelle F MotaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Benjamin JakobusModal Informática Ltda Almeida Godinho, 19, 304 Rio de Janeiro RJ 22741-140 Brazil.
Gileno Dos Santos de SousaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Filipe Pereira da CostaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Adriani L FelixInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Giulia D S FerrettiInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.
Fernando P AlmeidaNational Center for Structural Biology and Bioimaging (CENABIO), Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil.ORCID https://orcid.org/0000-0002-7352-9613
Yraima CordeiroFaculty of Pharmacy, Federal University of Rio de Janeiro Rio de Janeiro Brazil.ORCID https://orcid.org/0000-0003-4278-212X
Tuane C R G VieiraInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.ORCID https://orcid.org/0000-0002-3574-5411
Guilherme A P de OliveiraInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.ORCID https://orcid.org/0000-0002-0063-5888
Jerson L SilvaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro Rio de Janeiro RJ 21941-902 Brazil gaugusto@bioqmed.ufrj.br jerson@bioqmed.ufrj.br.ORCID https://orcid.org/0000-0001-9523-9441
Universidade Federal do Rio de Janeiro · BRUniversidade do Estado do Rio de Janeiro · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutant p53 tends to form aggregates with amyloid properties, especially amyloid oligomers inside the nucleus, which are believed to cause oncogenic gain-of-function (GoF). The mechanism of the formation of the aggregates in the nucleus remains uncertain. The present study demonstrated that the DNA-binding domain of p53 (p53C) underwent phase separation (PS) on the pathway to aggregation under various conditions. p53C phase separated in the presence of the crowding agent polyethylene glycol (PEG). Similarly, mutant p53C (M237I and R249S) underwent PS; however, the process evolved to a solid-like phase transition faster than that in the case of wild-type p53C. The data obtained by microscopy of live cells indicated that transfection of mutant full-length p53 into the cells tended to result in PS and phase transition (PT) in the nuclear compartments, which are likely the cause of the GoF effects. Fluorescence recovery after photobleaching (FRAP) experiments revealed liquid characteristics of the condensates in the nucleus. Mutant p53 tended to undergo gel- and solid-like phase transitions in the nucleus and in nuclear bodies demonstrated by slow and incomplete recovery of fluorescence after photobleaching. Polyanions, such as heparin and RNA, were able to modulate PS and PT

Identifiers

PMID34163823
PMCPMC8171334
OpenAlexW3157591981

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.